@article{4dd5389b7a3243b289deec530e13dc3d,
title = "The dissociation of glutamic dehydrogenase by reduced diphosphopyridine nucleotide (DPNH)",
author = "Carl Frieden",
note = "Funding Information: Although cross-reactivity of chymotrypsin and trypsin to certain substrates is not without parallel, it was not anticipated that m#g amounts of trypsin would necessarily produce a rapid hydrolysis of CTpNP. However, the rate curve obtained with trypsin was comparable to that observed with chymotrypsin and velocity was proportional to the trypsin concentration (Fig. i, B). The maximum rate of hydrolysis occurred at about pH 8. As was found for chymotrypsin, tryptic activity toward CTpNP was completely inhibited by diiso propylphosphorofluoridate. Thus, the use of CTpNP permits direct and rapid measurements of reaction rates utilizing quantities of chymotrypsin as low as 3 mpg/ml and amounts of trypsin as low as 7 m/zg/ml. This work has been supported in part by research grants A-727 and RG 4624 from the United States Public Health Service.",
year = "1958",
doi = "10.1016/0006-3002(58)90364-0",
language = "English",
volume = "27",
pages = "431--432",
journal = "BBA - Biochimica et Biophysica Acta",
issn = "0006-3002",
number = "C",
}